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3nsu
From Proteopedia
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| - | + | ==A Systematic Screen for Protein-Lipid Interactions in Saccharomyces cerevisiae== | |
| - | + | <StructureSection load='3nsu' size='340' side='right' caption='[[3nsu]], [[Resolution|resolution]] 2.00Å' scene=''> | |
| - | + | == Structural highlights == | |
| + | <table><tr><td colspan='2'>[[3nsu]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NSU OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NSU FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1btk|1btk]]</td></tr> | ||
| + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LIT2, SLM1, YIL105C ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3nsu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3nsu OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3nsu RCSB], [http://www.ebi.ac.uk/pdbsum/3nsu PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Protein-metabolite networks are central to biological systems, but are incompletely understood. Here, we report a screen to catalog protein-lipid interactions in yeast. We used arrays of 56 metabolites to measure lipid-binding fingerprints of 172 proteins, including 91 with predicted lipid-binding domains. We identified 530 protein-lipid associations, the majority of which are novel. To show the data set's biological value, we studied further several novel interactions with sphingolipids, a class of conserved bioactive lipids with an elusive mode of action. Integration of live-cell imaging suggests new cellular targets for these molecules, including several with pleckstrin homology (PH) domains. Validated interactions with Slm1, a regulator of actin polarization, show that PH domains can have unexpected lipid-binding specificities and can act as coincidence sensors for both phosphatidylinositol phosphates and phosphorylated sphingolipids. | ||
| - | + | A systematic screen for protein-lipid interactions in Saccharomyces cerevisiae.,Gallego O, Betts MJ, Gvozdenovic-Jeremic J, Maeda K, Matetzki C, Aguilar-Gurrieri C, Beltran-Alvarez P, Bonn S, Fernandez-Tornero C, Jensen LJ, Kuhn M, Trott J, Rybin V, Muller CW, Bork P, Kaksonen M, Russell RB, Gavin AC Mol Syst Biol. 2010 Nov 30;6:430. PMID:21119626<ref>PMID:21119626</ref> | |
| - | + | ||
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | == | + | <references/> |
| - | + | __TOC__ | |
| + | </StructureSection> | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
| - | [[Category: Aguilar-Gurrieri, C | + | [[Category: Aguilar-Gurrieri, C]] |
| - | [[Category: Fernandez-Tornero, C | + | [[Category: Fernandez-Tornero, C]] |
| - | [[Category: Gallego, O | + | [[Category: Gallego, O]] |
| - | [[Category: Gavin, A C | + | [[Category: Gavin, A C]] |
| - | [[Category: Muller, C | + | [[Category: Muller, C]] |
[[Category: Pleckstrin homology domain]] | [[Category: Pleckstrin homology domain]] | ||
[[Category: Signaling protein]] | [[Category: Signaling protein]] | ||
Revision as of 06:46, 19 December 2014
A Systematic Screen for Protein-Lipid Interactions in Saccharomyces cerevisiae
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